Summary:
The L2 protein is a component of the 50S subunit of the ribosome and is part of the peptidyltransferase center. L2 is highly evolutionarily conserved [Schmid84, Uhlein98].

L2 is required for the association of the 30S and 50S subunits [Diedrich00]; one end of the elongated L2 protein is located at the intersubunit interface of the 50S subunit [Willumeit01]. L2 is involved in binding of tRNA to both the A and P sites, and the His229 residue appears to be important for peptidyl-transferase activity of the ribosome [Diedrich00]. A conserved region within L2 is required for assembly of L16 into the 50S ribosomal subunit [Romero90]. Ribosome modulation factor binds near L2, L13, and S13 [Yoshida02b].

Summary:
The ribosome is a complex machinery that translates the genetic code.

A crystal structure of the E. coli ribosome has been determined at 3.5 Å resolution [Schuwirth05]. Additional crystal structures of the ribosome with tRNA bound in two functionally distinct states reveal how a ratchet-like motion of the small and large subunits contributes to translocation, termination of translation, and ribosome recycling [Zhang09b, Dunkle11].

Approximately eight molecules of Zn2+ are bound to the ribosome; therefore, it appears that a large fraction of intracellular Zn2+ is ribosome-associated [Hensley11].